Recombinant Human GLP2R protein

The glucagon-like peptide-2 receptor (GLP2R) is a class B G protein-coupled receptor (GPCR) that plays a critical role in regulating intestinal homeostasis, nutrient absorption, and mucosal repair. It is primarily expressed in the gastrointestinal tract, particularly in enteroendocrine cells, enteric neurons, and myofibroblasts. The receptor binds its endogenous ligand, glucagon-like peptide-2 (GLP-2), a 33-amino acid peptide derived from proglucagon. Activation of GLP2R triggers intracellular signaling cascades, predominantly via the Gαs-adenylyl cyclase pathway, leading to enhanced crypt cell proliferation, reduced apoptosis, and improved barrier function. These effects underscore its therapeutic potential in conditions like short bowel syndrome, inflammatory bowel disease, and chemotherapy-induced enteropathy.

Recombinant GLP2R proteins are engineered to study receptor-ligand interactions, signaling mechanisms, and drug discovery. Produced through heterologous expression systems (e.g., mammalian HEK293 or insect cells), recombinant GLP2R retains structural and functional integrity, enabling in vitro characterization. Researchers often fuse affinity tags (e.g., FLAG or His-tag) to facilitate purification and detection. Structural studies using cryo-EM and X-ray crystallography of recombinant GLP2R have provided insights into ligand-binding domains and activation conformations, aiding the design of GLP-2 analogs or small-molecule agonists. Challenges include maintaining receptor stability during purification and ensuring proper post-translational modifications critical for ligand binding. Current applications extend to high-throughput screening for therapeutics targeting metabolic and gastrointestinal disorders, highlighting its translational relevance in precision medicine.